ID   A0A6J2PKV2_COTGO        Unreviewed;       562 AA.
AC   A0A6J2PKV2;
DT   07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT   07-OCT-2020, sequence version 1.
DT   02-OCT-2024, entry version 19.
DE   RecName: Full=Cytosolic purine 5'-nucleotidase {ECO:0000256|ARBA:ARBA00040391};
DE            EC=2.7.1.77 {ECO:0000256|ARBA:ARBA00038866};
DE            EC=3.1.3.5 {ECO:0000256|ARBA:ARBA00012643};
DE            EC=3.1.3.99 {ECO:0000256|ARBA:ARBA00012894};
DE   AltName: Full=Cytosolic nucleoside phosphotransferase 5'N {ECO:0000256|ARBA:ARBA00042328};
GN   Name=nt5c2 {ECO:0000313|RefSeq:XP_029286683.1};
OS   Cottoperca gobio (Frogmouth) (Aphritis gobio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Notothenioidei; Bovichtidae; Cottoperca.
OX   NCBI_TaxID=56716 {ECO:0000313|Proteomes:UP000504630, ECO:0000313|RefSeq:XP_029286683.1};
RN   [1] {ECO:0000313|RefSeq:XP_029286683.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (JUN-2024) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AMP + inosine = adenosine + IMP; Xref=Rhea:RHEA:69596,
CC         ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:58053,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000256|ARBA:ARBA00036349};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CMP + inosine = cytidine + IMP; Xref=Rhea:RHEA:69592,
CC         ChEBI:CHEBI:17562, ChEBI:CHEBI:17596, ChEBI:CHEBI:58053,
CC         ChEBI:CHEBI:60377; Evidence={ECO:0000256|ARBA:ARBA00036204};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GMP + H2O = guanosine + phosphate; Xref=Rhea:RHEA:27714,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16750, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58115; Evidence={ECO:0000256|ARBA:ARBA00036695};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27715;
CC         Evidence={ECO:0000256|ARBA:ARBA00036695};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GMP + inosine = guanosine + IMP; Xref=Rhea:RHEA:69584,
CC         ChEBI:CHEBI:16750, ChEBI:CHEBI:17596, ChEBI:CHEBI:58053,
CC         ChEBI:CHEBI:58115; Evidence={ECO:0000256|ARBA:ARBA00036089};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + IMP = inosine + phosphate; Xref=Rhea:RHEA:27718,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:17596, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58053; EC=3.1.3.99;
CC         Evidence={ECO:0000256|ARBA:ARBA00036953};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27719;
CC         Evidence={ECO:0000256|ARBA:ARBA00036953};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + XMP = phosphate + xanthosine; Xref=Rhea:RHEA:28530,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:18107, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57464; Evidence={ECO:0000256|ARBA:ARBA00036213};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28531;
CC         Evidence={ECO:0000256|ARBA:ARBA00036213};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside + a ribonucleoside 5'-phosphate = a
CC         2'-deoxyribonucleoside 5'-phosphate + a ribonucleoside;
CC         Xref=Rhea:RHEA:19961, ChEBI:CHEBI:18254, ChEBI:CHEBI:18274,
CC         ChEBI:CHEBI:58043, ChEBI:CHEBI:65317; EC=2.7.1.77;
CC         Evidence={ECO:0000256|ARBA:ARBA00036260};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside +
CC         phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00035871};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12485;
CC         Evidence={ECO:0000256|ARBA:ARBA00035871};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dGMP + H2O = 2'-deoxyguanosine + phosphate;
CC         Xref=Rhea:RHEA:29379, ChEBI:CHEBI:15377, ChEBI:CHEBI:17172,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57673;
CC         Evidence={ECO:0000256|ARBA:ARBA00036911};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29380;
CC         Evidence={ECO:0000256|ARBA:ARBA00036911};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dGMP + inosine = 2'-deoxyguanosine + IMP;
CC         Xref=Rhea:RHEA:69580, ChEBI:CHEBI:17172, ChEBI:CHEBI:17596,
CC         ChEBI:CHEBI:57673, ChEBI:CHEBI:58053;
CC         Evidence={ECO:0000256|ARBA:ARBA00036593};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dIMP + H2O = 2'-deoxyinosine + phosphate;
CC         Xref=Rhea:RHEA:29383, ChEBI:CHEBI:15377, ChEBI:CHEBI:28997,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:61194;
CC         Evidence={ECO:0000256|ARBA:ARBA00036191};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29384;
CC         Evidence={ECO:0000256|ARBA:ARBA00036191};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dIMP + inosine = 2'-deoxyinosine + IMP; Xref=Rhea:RHEA:69572,
CC         ChEBI:CHEBI:17596, ChEBI:CHEBI:28997, ChEBI:CHEBI:58053,
CC         ChEBI:CHEBI:61194; Evidence={ECO:0000256|ARBA:ARBA00036258};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=inosine + UMP = IMP + uridine; Xref=Rhea:RHEA:69588,
CC         ChEBI:CHEBI:16704, ChEBI:CHEBI:17596, ChEBI:CHEBI:57865,
CC         ChEBI:CHEBI:58053; Evidence={ECO:0000256|ARBA:ARBA00036826};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR017434-2};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR017434-2};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}.
CC   -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family.
CC       {ECO:0000256|ARBA:ARBA00009589}.
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DR   RefSeq; XP_029286683.1; XM_029430823.1.
DR   AlphaFoldDB; A0A6J2PKV2; -.
DR   KEGG; cgob:115007821; -.
DR   InParanoid; A0A6J2PKV2; -.
DR   OrthoDB; 3626840at2759; -.
DR   Proteomes; UP000504630; Chromosome 1.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0008253; F:5'-nucleotidase activity; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046037; P:GMP metabolic process; IEA:UniProt.
DR   CDD; cd07522; HAD_cN-II; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR008380; HAD-SF_hydro_IG_5-nucl.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR016695; Pur_nucleotidase.
DR   NCBIfam; TIGR02244; HAD-IG-Ncltidse; 1.
DR   PANTHER; PTHR12103; 5'-NUCLEOTIDASE DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR12103:SF17; CYTOSOLIC PURINE 5'-NUCLEOTIDASE; 1.
DR   Pfam; PF05761; 5_nucleotid; 1.
DR   PIRSF; PIRSF017434; Purine_5'-nucleotidase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR017434-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR017434-2};
KW   Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000504630};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REGION          531..562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..562
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        52
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017434-1"
FT   ACT_SITE        54
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017434-1"
FT   BINDING         52
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017434-2"
FT   BINDING         54
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017434-2"
FT   BINDING         351
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017434-2"
SQ   SEQUENCE   562 AA;  65198 MW;  46F01AF7841AC5A4 CRC64;
     MTTSWSDRLQ NYADLPANMD GVTMKKYRRE PYHRVFVNRS LAMEKIKCFG FDMDYTLAVY
     KSPEYESLGF ELTVERLVSI GYPQELLSFV YDPSFPTRGL VFDTMYGNLL KVDAYGNILV
     CVHGFNFLRG PEIRERYPNK FIQRDDTERF YILNTLFNLP ETYLFACLVD FFSNCDRYTS
     CESGFKNGDL FMSYKSMFQD VRDAVDWVHF KGTLKEKTVE NLEKYVVRDG KLPLLLSRMN
     EVAKVFLATN SDYKYTDKIM NYLFDFPHGP KPGTSHRPWQ SYFDLILADA RKPLFFGEGT
     VLRQVDTTTG RLKIGTYTGP LQHGIVYSGG SSDIVCDLLG AKGKDIVYIG DHIFGDILKS
     KKRQGWRTFL VIPELAQELH VWTDKSSLFE ELQGLDIFLA ELYKHLDSSS NERPDISTIQ
     RRVKKVTHDM DMCYGMMGSL FRSGSRQTLF ASQVMRYADL YAASFINLLY YPFSYLFRAA
     HVLMPHESTV EHAHVDIDME SPLATRNRTH CSDCKDLECK RNQLTRSFSE IKPPNLFPQT
     PQEITHCHDE DDDEEEEEEE EE
//